title: Catalase-peroxidase activity of iron(III)-TAML activators of hydrogen peroxide.
abstract: Exceptionally high peroxidase-like and catalase-like activities of iron(III)-TAML activators of H 2O 2 ( 1: Tetra-Amidato-Macrocyclic-Ligand Fe (III) complexes [ F e{1,2-X 2C 6H 2-4,5-( NCOCMe 2 NCO) 2CR 2}(OH 2)] (-)) are reported from pH 6-12.4 and 25-45 degrees C. Oxidation of the cyclometalated 2-phenylpyridine organometallic complex, [Ru (II)( o-C 6H 4py)(phen) 2]PF 6 ( 2) or "ruthenium dye", occurs via the equation [ Ru II ] + 1/2 H 2 O 2 + H +-->(Fe III - TAML) [ Ru III ] + H 2 O, following a simple rate law rate = k obs (per)[ 1][H 2O 2], that is, the rate is independent of the concentration of 2 at all pHs and temperatures studied. The kinetics of the catalase-like activity (H 2 O 2 -->(Fe III - TAML) H 2 O + 1/2 O 2) obeys a similar rate law: rate = k obs (cat)[ 1][H 2O 2]). The rate constants, k obs (per) and k obs (cat), are strongly and similarly pH dependent, with a maximum around pH 10. Both bell-shaped pH profiles are quantitatively accounted for in terms of a common mechanism based on the known speciation of 1 and H 2O 2 in this pH range. Complexes 1 exist as axial diaqua species [FeL(H 2O) 2] (-) ( 1 aqua) which are deprotonated to afford [FeL(OH)(H 2O)] (2-) ( 1 OH) at pH 9-10. The pathways 1 aqua + H 2O 2 ( k 1), 1 OH + H 2O 2 ( k 2), and 1 OH + HO 2 (-) ( k 4) afford one or more oxidized Fe-TAML species that further rapidly oxidize the dye (peroxidase-like activity) or a second H 2O 2 molecule (catalase-like activity). This mechanism is supported by the observations that (i) the catalase-like activity of 1 is controllably retarded by addition of reducing agents into solution and (ii) second order kinetics in H 2O 2 has been observed when the rate of O 2 evolution was monitored in the presence of added reducing agents. The performances of the 1 complexes in catalyzing H 2O 2 oxidations are shown to compare favorably with the peroxidases further establishing Fe (III)-TAML activators as miniaturized enzyme replicas with the potential to greatly expand the technological utility of hydrogen peroxide.
authors.affiliation: Department of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, USA.
authors.forename: Anindya
authors.initials: A
authors.lastname: Ghosh
authors.forename: Douglas A
authors.initials: DA
authors.lastname: Mitchell
authors.forename: Arani
authors.initials: A
authors.lastname: Chanda
authors.forename: Alexander D
authors.initials: AD
authors.lastname: Ryabov
authors.forename: Delia Laura
authors.initials: DL
authors.lastname: Popescu
authors.forename: Erin C
authors.initials: EC
authors.lastname: Upham
authors.forename: Gregory J
authors.initials: GJ
authors.lastname: Collins
authors.forename: Terrence J
authors.initials: TJ
authors.lastname: Collins
mesh_terms: D002232:Carbocyanines / Q000737:chemistry; D002374:Catalase / Q000737:chemistry*; D005290:Ferric Compounds / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D058085:Iron Compounds / Q000737:chemistry*; D007700:Kinetics; D047028:Macrocyclic Compounds / Q000737:chemistry*; D008665:Metalloporphyrins / Q000737:chemistry; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000737:chemistry*; D012428:Ruthenium / Q000737:chemistry
chemical_list: D002232:Carbocyanines; D005290:Ferric Compounds; D058085:Iron Compounds; D047028:Macrocyclic Compounds; D008665:Metalloporphyrins; C517362:iron-3,3,6,6,9,9-hexamethyl-3,4,8,9-tetrahydro-1H-1,4,8,11-benzotetraazacyclotridecine-2,5,7,10(6H,11H)-tetraone; D012428:Ruthenium; C019071:quinaldine blue; D006861:Hydrogen Peroxide; D002374:Catalase; D009195:Peroxidase